ArticleJournal of immunological methods2019
Expression and characterization of soluble epitope-defined major histocompatibility complex (MHC) from stable eukaryotic cell lines.
Article in Journal of immunological methods, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 8 citations in OpenAlex.
- Peptide exchange-competent class I MHC molecules produced in eukaryotic cells for rapid production of MHC multimers.Journal of immunology (Baltimore, Md. : 1950) · 2026Article
- Non-cognate CD8 Binding to MHC I Promotes Positive Selection of an MHC-E Restricted CD8 T Cell Population.European journal of immunology · 2026Article
- Modeling antibody drug conjugate potential using a granzyme B antibody fusion protein.BMC biology · 2024Article
- MediMer: a versatile do-it-yourself peptide-receptive MHC class I multimer platform for tumor neoantigen-specific T cell detection.Frontiers in immunology · 2023Article
- Production of soluble pMHC-I molecules in mammalian cells using the molecular chaperone TAPBPR.Protein engineering, design & selection : PEDS · 2019Article
- MHC-I peptide binding activity assessed by exchange after cleavage of peptide covalently linked to β2-microglobulin.Analytical biochemistry · 2019Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
MHC class I-specific reagents such as fluorescently-labeled multimers (e.g., tetramers) have greatly advanced the understanding of CD8+ T cells under normal and diseased states. However, recombinant MHC class I components (comprising MHC class I heavy chain and β2 microglobulin) are usually produced in bacteria following a lengthy purification protocol that requires additional non-covalent folding steps with exogenous peptide for complete molecular assembly. We have provided an alternative and rapid approach to generating soluble and fully-folded MHC class I molecules in eukaryotic cell lines (such as CHO cells) using a Sleeping Beauty transposon system. Importantly, this method culminates in generating stable cell lines that reliably secrete epitope-defined MHC class I molecules into the tissue media for convenient purification and eventual biotinylation/multimerization. Additionally, MHC class I components are covalently linked, providing the opportunity to produce a diverse set of CD8+ T cell-specific reagents bearing peptides with various affinities to MHC class I.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.